Crystallization and preliminary X-ray study of alkaline beta-mannanase from the alkaliphilic Bacillus sp. N16-5.
The catalytic domain of an alkaline beta-mannanase from the alkaliphilic Bacillus sp. N16-5 has been expressed and purified. The recombinant enzyme was crystallized using the hanging-drop vapour-diffusion method at 298 K. X-ray diffraction data were collected to 1.6 A resolution. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 59.03, b = 63.31, c = 83.34 A. Initial phasing was carried out by molecular replacement using the three-dimensional structure of a mannanase from the alkaliphilic Bacillus sp. JAMB602 as a search model.
Zhao
Yueju
Y
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Zhang
Yunhua
Y
Gao
Feng
F
Xue
Yanfen
Y
Zeng
Yan
Y
Ma
Yanhe
Y
D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D003460:Crystallization; D017931:DNA Primers; D004269:DNA, Bacterial / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D010957:Plasmids; D014961:X-Ray Diffraction / Q000379:methods; D044902:beta-Mannosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D017931:DNA Primers; D004269:DNA, Bacterial; D005656:Fungal Proteins; D010940:Plant Proteins; D044902:beta-Mannosidase